ECOLI:LON

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Species (Taxon ID)	Escherichia coli (strain K12). (taxon:83333)
Gene Name(s)	lon ( synonyms: capR, deg, lopA, muc )
Protein Name(s)	Lon protease ATP-dependent protease La
External Links
UniProt Identifier	LON_ECOLI
UniProt Accessions	P0A9M0, P08177, P78219, Q2MBY7,
EMBL	L12349, M38347, L20572, J03896, U82664, U00096, AP009048, M10153,
PIR	A23101, G64773,
RefSeq	AP_001089.1, NP_414973.1,
PDB	1QZM, 1RR9, 1RRE, 2ANE, 3LJC,
Pfam	PF00004, PF02190, PF05362,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0005737	cytoplasm		IDA: Inferred from Direct Assay		C	Source: EcoliWiki
	GO:0005524	ATP binding		IPI: Inferred from Physical Interaction		F	Source: EcoliWiki
	GO:0004176	ATP-dependent peptidase activity		IDA: Inferred from Direct Assay		F	Source: EcoliWiki
	GO:0003677	DNA binding		IDA: Inferred from Direct Assay		F	Source: EcoliWiki
	GO:0004252	serine-type endopeptidase activity		IMP: Inferred from Mutant Phenotype		F	Source: EcoliWiki
	GO:0006508	proteolysis		IDA: Inferred from Direct Assay		P	Source: EcoliWiki
	GO:0009408	response to heat		IEP: Inferred from Expression Pattern		P	Source: EcoliWiki
	GO:0009411	response to UV	PMID:4934518^[1]	IMP: Inferred from Mutant Phenotype		P	table 5	complete
	GO:0009408	response to heat	PMID:6436819^[2]	IEP: Inferred from Expression Pattern		P	Table 1. shows upregulation of Lon in response to heat exposure (42C)	complete
	GO:0006508	proteolysis	PMID:6436819^[2]	IMP: Inferred from Mutant Phenotype		P	Fig. 1 and 2 show decreased proteolytic activity in the mutant phenotype	complete
	GO:0045471	response to ethanol	PMID:6436819^[2]	IEP: Inferred from Expression Pattern		P	Table 1. shows enhanced Lon expression in the presence of ethanol (4%)	complete
	GO:0009411	response to UV	PMID:6436819^[2]	IMP: Inferred from Mutant Phenotype		P	Table 3. Increased UV sensitivity in mutant lon	complete
	GO:0000166	nucleotide binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003593	F
	GO:0000166	nucleotide binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0547	F
	GO:0003677	DNA binding	PMID:8995294^[3]	IDA: Inferred from Direct Assay		F
	GO:0004176	ATP-dependent peptidase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003111	F
	GO:0004176	ATP-dependent peptidase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR004815	F
	GO:0004176	ATP-dependent peptidase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008268	F
	GO:0004176	ATP-dependent peptidase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008269	F
	GO:0004176	ATP-dependent peptidase activity	PMID:6458036^[4]	IDA: Inferred from Direct Assay		F
	GO:0004176	ATP-dependent peptidase activity	PMID:9720920^[5]	IDA: Inferred from Direct Assay		F
	GO:0004252	serine-type endopeptidase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008268	F
	GO:0004252	serine-type endopeptidase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008269	F
	GO:0004252	serine-type endopeptidase activity	PMID:15606774^[6]	IMP: Inferred from Mutant Phenotype		F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003959	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR004815	F
	GO:0005524	ATP binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0067	F
	GO:0005524	ATP binding	GO_REF:0000033		PANTHER:PTHR10046_AN0	F
	GO:0005524	ATP binding	PMID:15037242^[7]	IPI: Inferred from Physical Interaction		F
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C
	GO:0005737	cytoplasm	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0086	C
	GO:0005737	cytoplasm	PMID:8995294^[3]	IDA: Inferred from Direct Assay		C
	GO:0006508	proteolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003111	P
	GO:0006508	proteolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR004815	P
	GO:0006508	proteolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008268	P
	GO:0006508	proteolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008269	P
	GO:0006508	proteolysis	PMID:6458036^[4]	IDA: Inferred from Direct Assay		P
	GO:0006515	misfolded or incompletely synthesized protein catabolic process	GO_REF:0000033		PANTHER:PTHR10046_AN0	P
	GO:0006950	response to stress	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0346	P
	GO:0006950	response to stress	PMID:6330035^[8]	IEP: Inferred from Expression Pattern		P
	GO:0008233	peptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0645	F
	GO:0008236	serine-type peptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0720	F
	GO:0009295	nucleoid	GO_REF:0000033		PANTHER:PTHR10046_AN0	C
	GO:0009408	response to heat	PMID:8349564^[9]	IEP: Inferred from Expression Pattern		P
	GO:0016787	hydrolase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0378	F
	GO:0017111	nucleoside-triphosphatase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003593	F
	GO:0043565	sequence-specific DNA binding	GO_REF:0000033		PANTHER:PTHR10046_AN0	F
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Takano T (1971) Bacterial mutants defective in plasmid formation: requirement for the lon + allele. Proc Natl Acad Sci U S A 68: 1469-73 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Goff SA et al. (1984) Heat shock regulatory gene htpR influences rates of protein degradation and expression of the lon gene in Escherichia coli. Proc Natl Acad Sci U S A 81: 6647-51 PubMed GONUTS page
↑ ^3.0 ^3.1 Fu GK et al. (1997) Bacterial protease Lon is a site-specific DNA-binding protein. J Biol Chem 272: 534-8 PubMed GONUTS page
↑ ^4.0 ^4.1 Charette MF et al. (1981) ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12. Proc Natl Acad Sci U S A 78: 4728-32 PubMed GONUTS page
↑ Rasulova FS et al. (1998) The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity. FEBS Lett 432: 179-81 PubMed GONUTS page
↑ Rotanova TV et al. (2004) Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains. Eur J Biochem 271: 4865-71 PubMed GONUTS page
↑ Botos I et al. (2004) Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution. J Struct Biol 146: 113-22 PubMed GONUTS page
↑ Phillips TA et al. (1984) lon gene product of Escherichia coli is a heat-shock protein. J Bacteriol 159: 283-7 PubMed GONUTS page
↑ Chuang SE & Blattner FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J Bacteriol 175: 5242-52 PubMed GONUTS page

[PMID:4934518-0] Takano T (1971) Bacterial mutants defective in plasmid formation: requirement for the lon + allele. Proc Natl Acad Sci U S A 68: 1469-73 PubMed GONUTS page

[PMID:6436819-1] 2.0 ^2.1 ^2.2 ^2.3 Goff SA et al. (1984) Heat shock regulatory gene htpR influences rates of protein degradation and expression of the lon gene in Escherichia coli. Proc Natl Acad Sci U S A 81: 6647-51 PubMed GONUTS page

[PMID:8995294-2] 3.0 ^3.1 Fu GK et al. (1997) Bacterial protease Lon is a site-specific DNA-binding protein. J Biol Chem 272: 534-8 PubMed GONUTS page

[PMID:6458036-3] 4.0 ^4.1 Charette MF et al. (1981) ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12. Proc Natl Acad Sci U S A 78: 4728-32 PubMed GONUTS page

[PMID:9720920-4] Rasulova FS et al. (1998) The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity. FEBS Lett 432: 179-81 PubMed GONUTS page

[PMID:15606774-5] Rotanova TV et al. (2004) Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains. Eur J Biochem 271: 4865-71 PubMed GONUTS page

[PMID:15037242-6] Botos I et al. (2004) Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution. J Struct Biol 146: 113-22 PubMed GONUTS page

[PMID:6330035-7] Phillips TA et al. (1984) lon gene product of Escherichia coli is a heat-shock protein. J Bacteriol 159: 283-7 PubMed GONUTS page

[PMID:8349564-8] Chuang SE & Blattner FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J Bacteriol 175: 5242-52 PubMed GONUTS page

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ECOLI:LON

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